Adsorption behaviour of statherin and a statherin peptide onto hydroxyapatite and silica surfaces studied by in situ ellipsometry

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Adsorption behaviour of statherin and a statherin peptide onto hydroxyapatite and silica surfaces studied by in situ ellipsometry

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Publication Article, peer reviewed scientific
Title Adsorption behaviour of statherin and a statherin peptide onto hydroxyapatite and silica surfaces studied by in situ ellipsometry
Author(s) Santos, Olga ; Kosoric, Jelena ; Hector, Mark P ; Anderson, Paul ; Lindh, Liselott
Date 2008
English abstract
The salivary protein statherin is known to adsorb selectively onto hydroxyapatite (HA), which constitutes the main mineral of the tooth enamel. This adsorption is believed to be crucial for its function as an inhibitor of primary (spontaneous) and secondary (crystal growth) precipitation of calcium phosphate salts present in saliva. A fragment corresponding to the first 21 N-terminus amino acids of statherin (StN21) was previously found to reduce the rate of demineralization of HA. Therefore, the interfacial properties of this peptide and statherin onto silica, hydrophobized silica and HA discs was studied by in situ ellipsometry. Their reversibility induced by dilution and elutability induced by buffer and sodium dodecyl sulfate (SDS) was also determined. The results revealed that statherin adsorbed at a greater extent onto the HA as compared to StN21, suggesting that the hydrogen bonding between the uncharged polar residues at the C-terminal region of statherin and HA contributes to its adsorption. However, on both silica surfaces the peptide adsorption appeared to proceed in a similar way. Onto the hydrophobized silica the adsorption of both peptides was suggested to occur either via multilayer formation or adsorption of aggregates from solution, while onto the hydrophilic silica adsorption of peptide aggregates from solution was the suggested mechanism. Further, both peptides were observed to be strongly adsorbed onto HA, even after SDS treatment, in comparison to the layers adsorbed onto hydrophobized silica. Both peptide layers were found to be weakly adsorbed onto the hydrophilic silica surface as they were totally removed by buffer dilution.
DOI http://dx.doi.org/10.1016/j.jcis.2007.11.015 (link to publisher's fulltext)
Host/Issue Journal of colloid and interface science;2
Volume 318
ISSN 0021-9797
Pages 175-182
Language eng (iso)
Subject(s) Medicine
Research Subject Categories::MEDICINE
Research Subject Categories::TECHNOLOGY
Handle http://hdl.handle.net/2043/7472 (link to this page)

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